期刊
CELL REPORTS
卷 25, 期 11, 页码 3136-+出版社
CELL PRESS
DOI: 10.1016/j.celrep.2018.11.067
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资金
- NIH [NIH/NIAID/R01AI095366, NIH/NIAID/2R01AI095436, NIH/NIAID/R21AI117331-01]
- Defense Threat Reduction Agency Awards [DTRA HDTRA 1-15-1-0047, DTRA HDTRA 1-15-1-0013]
- Bill and Melinda Gates Foundation through Collaboration for AIDS Vaccine Discovery Grant [OPP1115782]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R21AI117331, R01AI095366, R01AI095436] Funding Source: NIH RePORTER
Alphaviruses are enveloped pathogens that cause arthritis and encephalitis. Here, we report a 4.4-angstrom cryo-electron microscopy (cryo-EM) structure of eastern equine encephalitis virus (EEEV), an alphavirus that causes fatal encephalitis in humans. Our analysis provides insights into viral entry into host cells. The envelope protein E2 showed a binding site for the cellular attachment factor heparan sulfate. The presence of a cryptic E2 glycan suggests how EEEV escapes surveillance by lectin-expressing myeloid lineage cells, which are sentinels of the immune system. A mechanism for nucleocapsid core release and disassembly upon viral entry was inferred based on pH changes and capsid dissociation from envelope proteins. The EEEV capsid structure showed a viral RNA genome binding site adjacent to a ribosome binding site for viral genome translation following genome release. Using five Fab-EEEV complexes derived from neutralizing antibodies, our investigation provides insights into EEEV host cell interactions and protective epitopes relevant to vaccine design.
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